Evidence map›Paper›PMID 8917565›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

NADPH-oxidase and a hydrogen peroxide-sensitive K+ channel may function as an oxygen sensor complex in airway chemoreceptors and small cell lung carcinoma cell lines.

D Wang, C Youngson, V Wong, H Yeger, M C Dinauer, E Vega-Saenz Miera, B Rudy, E Cutz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 194 citations in OpenAlex.

  1. Article
  2. HInternational journal of molecular sciences · 2025
    Article
  3. The Coding Logic of Interoception.Annual review of physiology · 2024
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Functional Exploration of the Pulmonary NEB ME.Advances in anatomy, embryology, and cell biology · 2021
    Article
  9. Pulmonary Sensory Receptors.Advances in anatomy, embryology, and cell biology · 2021
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. The role of redox changes in oxygen sensing.Respiratory physiology & neurobiology · 2010
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 2 countries.

D WangDepartment of Pathology, Hospital for Sick Children, Toronto, ON, Canada.
C Youngson
V Wong
H Yeger
M C Dinauer
E Vega-Saenz Miera
B Rudy
E Cutz
University of Toronto · CA

Funding

EXPRESSION AND FUNCTION OF K+ CHANNEL GENES IN THE CNSR01NS030989 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RUDY, BERNARDO · 1992 to 2015
$6.3M
NINDS NIH HHS NS30989NINDS NIH HHS R01 NS030989
6 · The paper itself

Abstract

Pulmonary neuroepithelial bodies (NEB) are widely distributed throughout the airway mucosa of human and animal lungs. Based on the observation that NEB cells have a candidate oxygen sensor enzyme complex (NADPH oxidase) and an oxygen-sensitive K+ current, it has been suggested that NEB may function as airway chemoreceptors. Here we report that mRNAs for both the hydrogen peroxide sensitive voltage gated potassium channel subunit (KH2O2) KV3.3a and membrane components of NADPH oxidase (gp91phox and p22phox) are coexpressed in the NEB cells of fetal rabbit and neonatal human lungs. Using a microfluorometry and dihydrorhodamine 123 as a probe to assess H2O2 generation, NEB cells exhibited oxidase activity under basal conditions. The oxidase in NEB cells was significantly stimulated by exposure to phorbol esther (0.1 microM) and inhibited by diphenyliodonium (5 microM). Studies using whole-cell voltage clamp showed that the K+ current of cultured fetal rabbit NEB cells exhibited inactivating properties similar to KV3.3a transcripts expressed in Xenopus oocyte model. Exposure of NEB cells to hydrogen peroxide (H2O2, the dismuted by-product of the oxidase) under normoxia resulted in an increase of the outward K+ current indicating that H2O2 could be the transmitter modulating the O2-sensitive K+ channel. Expressed mRNAs or corresponding protein products for the NADPH oxidase membrane cytochrome b as well as mRNA encoding KV3.3a were identified in small cell lung carcinoma cell lines. The studies presented here provide strong evidence for an oxidase-O2 sensitive potassium channel molecular complex operating as an O2 sensor in NEB cells, which function as chemoreceptors in airways and in NEB related tumors. Such a complex may represent an evolutionary conserved biochemical link for a membrane bound O2-signaling mechanism proposed for other cells and life forms.

Indexed as

Membrane Transport ProteinsAnimalsAnimals, NewbornCarcinoma, Small CellCell LineChemoreceptor CellsEpitheliumFetusHumansHydrogen PeroxideKineticsLungLung NeoplasmsMembrane GlycoproteinsMembrane PotentialsModels, BiologicalCYBA protein, humanCYBB protein, humanHydrogen PeroxideMembrane GlycoproteinsMembrane Transport ProteinsNADPH DehydrogenaseNADPH Oxidase 2NADPH OxidasesOxygenPhosphoproteinsPotassium Channels

Identifiers

PMID8917565
PMCPMC24067
OpenAlexW1978241980

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.